Analytical Data
-
Gene name
EphA5
-
简介
The EPHA5 protein is a receptor tyrosine kinase that promiscuously binds to the GPI-anchored ephrin-A ligand to initiate bidirectional signaling. It is involved in forward and reverse signaling pathways, and EFNA5 may serve as its cognate ligand. EPHA5 Protein, Human (HEK293, His) is the recombinant human-derived EPHA5 protein, expressed by HEK293 , with C-His labeled tag.
- Application
-
Alternative Names
EHK-1; EK7; BSK; EHK1; HEK7; TYRO4; EphA5; Rek7; TYRO4HEK7CEK7
-
Species
Human
-
Source
HEK293
-
Tag
C-8*His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P54756-1
-
Expression Region
A26-P573
-
Protein Length
Extracellular Domain
-
Molecular Weight
68-80 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
EphA5 is a member of the Eph receptor tyrosine kinase family, which plays a pivotal role in various biological processes, including cell adhesion, axon guidance, and the development of the nervous system. Research into EphA5 has gained substantial attention due to its involvement in significant diseases, particularly in cancer and neurological disorders. Studies have shown that EphA5 can influence tumor progression, metastasis, and overall oncogenic signaling pathways. Furthermore, it has been implicated in the modulation of synaptic plasticity and neural network formation, highlighting its importance in both physiology and pathology. The ability to produce EphA5 as a recombinant protein has opened avenues for therapeutic applications, enabling detailed studies of its structural and functional properties. Investigating the interactions and signaling pathways mediated by EphA5 through recombinant protein approaches can provide insights into its roles in disease. Consequently, understanding EphA5 at both molecular and cellular levels is crucial for developing targeted therapies that could improve treatment outcomes for cancer and neurodegenerative conditions. Therefore, the characterization of EphA5 recombinant protein is an essential step towards elucidating its biological functions and therapeutic potentials.
